The Oct-1 POU-specific domain can stimulate small nuclear RNA gene transcription by stabilizing the basal transcription complex SNAPc.

Détails

ID Serval
serval:BIB_029656FD7075
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The Oct-1 POU-specific domain can stimulate small nuclear RNA gene transcription by stabilizing the basal transcription complex SNAPc.
Périodique
Molecular and Cellular Biology
Auteur(s)
Mittal V., Cleary M.A., Herr W., Hernandez N.
ISSN
0270-7306[print], 0270-7306[linking]
Statut éditorial
Publié
Date de publication
05/1996
Volume
16
Numéro
5
Pages
1955-1965
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
The RNA polymerase II and III human small nuclear RNA promoters have a common basal element, the proximal sequence element, which binds the TATA box-binding protein-containing complex SNAPc. They also contain an enhancer characterized by a highly conserved octamer sequence, which constitutes a binding site for the broadly expressed POU domain transcription factor Oct-1. The POU domain is a bipartite DNA-binding domain consisting of a POU-homeo (POUH) domain and a POU-specific (POUs) domain joined by a flexible linker. Here, we show that the Oct-1 POU domain but not the related Pit-1 POU domain can facilitate the binding of SNAPc to the proximal sequence element, and activate transcription. The effect is probably mediated by protein-protein contacts, and 1 of 30 amino acid differences between the Oct-1 and Pit-1 POUs domains is the key determinant for the differential interaction with SNAPc and the ability to activate transcription. These results show that a function that is the hallmark of activation domains, namely, recruitment of a basal transcription complex resulting in activation of transcription, can be performed by a DNA-binding domain. In this case, subtle changes between activator DNA-binding domains, as subtle as a single amino acid difference, can profoundly affect interaction with the basal transcription machinery.
Mots-clé
Amino Acid Sequence, Base Sequence, Binding Sites, Cloning, Molecular, Conserved Sequence, DNA-Binding Proteins/biosynthesis, DNA-Binding Proteins/metabolism, Genes, Homeobox, Glutathione Transferase/biosynthesis, Glutathione Transferase/metabolism, Homeodomain Proteins/biosynthesis, Homeodomain Proteins/metabolism, Host Cell Factor C1, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Octamer Transcription Factor-1, Octamer Transcription Factor-2, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Genetic, RNA Polymerase I/metabolism, RNA Polymerase II/metabolism, RNA, Small Nuclear/biosynthesis, Recombinant Fusion Proteins/biosynthesis, Recombinant Fusion Proteins/metabolism, Sequence Homology, Amino Acid, TATA Box, TATA-Box Binding Protein, Transcription Factor Pit-1, Transcription Factors/biosynthesis, Transcription Factors/metabolism, Transcription, Genetic
Pubmed
Web of science
Création de la notice
24/01/2008 16:36
Dernière modification de la notice
20/08/2019 13:24
Données d'usage